PD1L2_HUMAN - dbPTM
PD1L2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PD1L2_HUMAN
UniProt AC Q9BQ51
Protein Name Programmed cell death 1 ligand 2
Gene Name PDCD1LG2
Organism Homo sapiens (Human).
Sequence Length 273
Subcellular Localization Isoform 3: Secreted .
Isoform 2: Endomembrane system
Single-pass type I membrane protein .
Isoform 1: Cell membrane
Single-pass type I membrane protein .
Protein Description Involved in the costimulatory signal, essential for T-cell proliferation and IFNG production in a PDCD1-independent manner. Interaction with PDCD1 inhibits T-cell proliferation by blocking cell cycle progression and cytokine production (By similarity)..
Protein Sequence MIFLLLMLSLELQLHQIAALFTVTVPKELYIIEHGSNVTLECNFDTGSHVNLGAITASLQKVENDTSPHRERATLLEEQLPLGKASFHIPQVQVRDEGQYQCIIIYGVAWDYKYLTLKVKASYRKINTHILKVPETDEVELTCQATGYPLAEVSWPNVSVPANTSHSRTPEGLYQVTSVLRLKPPPGRNFSCVFWNTHVRELTLASIDLQSQMEPRTHPTWLLHIFIPFCIIAFIFIATVIALRKQLCQKLYSSKDTTKRPVTTTKREVNSAI
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
9PhosphorylationIFLLLMLSLELQLHQ
HHHHHHHHHHHHHHH
13.0624719451
22PhosphorylationHQIAALFTVTVPKEL
HHHHHHHEEEECCEE
19.0024719451
37N-linked_GlycosylationYIIEHGSNVTLECNF
EEEECCCCEEEEEEC
35.07UniProtKB CARBOHYD
64N-linked_GlycosylationASLQKVENDTSPHRE
EEEHHHHCCCCCHHH
61.93UniProtKB CARBOHYD
114PhosphorylationGVAWDYKYLTLKVKA
EEEECCEEEEEEEHE
9.93-
116PhosphorylationAWDYKYLTLKVKASY
EECCEEEEEEEHEEE
22.80-
128PhosphorylationASYRKINTHILKVPE
EEEEECEEEEEECCC
17.48-
157N-linked_GlycosylationLAEVSWPNVSVPANT
EEEEECCCEECCCCC
32.22UniProtKB CARBOHYD
159PhosphorylationEVSWPNVSVPANTSH
EEECCCEECCCCCCC
29.08-
163N-linked_GlycosylationPNVSVPANTSHSRTP
CCEECCCCCCCCCCC
35.72UniProtKB CARBOHYD
165PhosphorylationVSVPANTSHSRTPEG
EECCCCCCCCCCCCC
21.19-
167PhosphorylationVPANTSHSRTPEGLY
CCCCCCCCCCCCCEE
37.30-
169PhosphorylationANTSHSRTPEGLYQV
CCCCCCCCCCCEEEE
28.8029978859
174PhosphorylationSRTPEGLYQVTSVLR
CCCCCCEEEEEEEEE
16.2829978859
177PhosphorylationPEGLYQVTSVLRLKP
CCCEEEEEEEEEECC
9.5229978859
178PhosphorylationEGLYQVTSVLRLKPP
CCEEEEEEEEEECCC
21.9429978859
189N-linked_GlycosylationLKPPPGRNFSCVFWN
ECCCCCCCEEEEEEC
38.81UniProtKB CARBOHYD

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PD1L2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PD1L2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PD1L2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PD1L2_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PD1L2_HUMAN

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Related Literatures of Post-Translational Modification

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